No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
COP1 overexpression inhibits p53 expression induced by fludarabine and promotes ubiquitin-mediated p53 degradation in chronic lymphocytic leukemia cells.
miR-103 blocked PI3K/AKT signal pathway by regulation of COP1. These data indicated that miR-103 was up-regulated in drug resistant cells and it may regulate ADR-resistance by regulation of COP1 in AML cells.
COP1 regulates human breast cancer cell proliferation and apoptosis in a p53-dependent manner.The COP1-mediated degradation of p53 regulates cancer cell growth and apoptosis.
that COP1 may play a role in promoting glioma cell proliferation by interacting with and downregulating tumor suppressor p53 rather than oncogenic protein c-JUN
COP1 forms complex with p53 protein and plays a role in p53 down-regulation.
Authors demonstrate that mtp53 prevents the COP1/DET1 complex from ubiquitinating ETS2 and thereby marking it for destruction. Authors show that mtp53 destabilizes DET1 and also disrupts the DET1/ETS2 complex thereby preventing ETS2 degradation.
STK40 binds the COP1 WD40 domain using a VPD/E motif in its C-terminal tail.
In conclusion, miR-214 functions as a tumor suppressor by regulating the RFWD2-p53 cascade, thus delivery of miR-214 analogs could be a potential adjunct therapy in breast cancer harboring wild type p53.
the reduced expression of COP1 and the upregulated expression of ETV1 in RCC tissue samples, which was associated with a high tumor-node-metastasis stage of RCC. Furthermore, the overexpression of COP1 in the RCC ACHN cells inhibited the migration and invasion of ACHN cells, and downregulated ETV1 and MMP7 expression levels.
COP1 expression was an independent predictor of overall survival.
protein level changes lead to increased sensitivity toward cisplatin treatment, implicating that huCOP1 plays a positive role in maintaining genome integrity in human keratinocytes.
the present study revealed that COP1 plays an important role in CLL cell proliferation and tumorigenicity, and may be a useful indicator of the chronic lymphocytic leukemia processes.
COP1 directly interacts with p27 through a VP motif on p27 and functions as an E3 ligase of p27 to accelerate the ubiquitin-mediated degradation of p27. COP1-p27 axis deregulation is involved in tumorigenesis.
COP1 overexpression leads to the cytoplasmic distribution of p27, thereby accelerating p27 degradation.
COP1 negatively regulates ETV1 in patients with triple-negative breast cancer.
changes in the expression of fast-responding early genes is modulated by huCOP1 in keratinocytes upon UVB irradiation
TRIB2 associated-ubiquitin E3 ligases beta-transducin repeat-containing E3 ubiquitin protein ligase (beta-TrCP), COP1 and Smad ubiquitination regulatory factor 1 (Smurf1) reduced TCF4/beta-Catenin expression, and these effects could be enhanced by TRIB2.
Phosphorylation of the ETS1 and ETS2 transcriptional oncoproteins at specific serine or threonine residues creates binding sites for the COP1 tumor suppressor protein.
while the role of COP1 in malignancies is controversial, our current data support that COP1 acts as a tumor suppressor in gastric cancer.
co-expressing COP1 and active GSK3beta blocked in vitro cell growth/migration and in vivo metastasis of invasive breast cancer cells.
Prenatal inactivation of Rfwd2 gene in the lung epithelium led to a striking halt in branching morphogenesis shortly after secondary branch formation.
Study shows that post-translational regulation of the transcription factors ETV1, ETV4, and ETV5 by the ubiquitin ligase COP1 (also called RFWD2) in beta cells is critical for insulin secretion. Mice lacking COP1 in beta cells developed diabetes due to insulin granule docking defects that were fully rescued by genetic deletion of Etv1, Etv4, and Etv5.
These results indicate that COP1 and Trib1 act as an oncoprotein complex functioning upstream of C/EBPalpha, and its ligase activity is crucial for leukemogenesis.
COP1 physically interacted with PTP1B and suppressed PTP1B phosphatase activity as well as the association of PTP1B with IRbeta.
Modulation of fatty acid synthase degradation by concerted action of p38 MAP kinase, E3 ligase COP1, and SH2-tyrosine phosphatase Shp2.
the ubiquitin ligase COP1 (also known as RFWD2) is a tumour suppressor that negatively regulates ETV1, ETV4 and ETV5; ETV1, which is mutated in prostate cancer more often, was degraded after being ubiquitinated by COP1
Cop1 is a tumor suppressor that functions, at least in part, by antagonizing c-Jun oncogenic activity.
Rfwd2 is associated with acute lung injury
description of a pathway in which Tribbles 3 (TRB3) stimulates lipolysis by triggering the degradation of acetyl-coenzyme A carboxylase (ACC) in adipose tissue; TRB3 promoted ACC ubiquitination through an association with the E3 ubiquitin ligase COP1
Disruption of the COP1-mediated proteolysis by ionizing radiation leads to MTA1 stabilization.
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1 (By similarity).
E3 ubiquitin-protein ligase RFWD2
, RING finger and WD repeat domain protein 2
, RING finger protein 200
, constitutive photomorphogenesis protein 1 homolog
, constitutive photomorphogenic protein (COP1)
, putative ubiquitin ligase COP1
, constitutive photomorphogenic protein 1
, ring finger and WD repeat domain 2